Recombinant Human VEGF 165 GMP Protein, CF: R&D Systems

Recombinant Human VEGF 165 GMP Protein, CF

Animal Component Free Process.
  
  • Purity
    >97%, by SDS-PAGE with silver staining.
  • Endotoxin Level
    <0.01 EU per 1 μg of the protein by the LAL method.
  • Activity
    Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323. The ED50 for this effect is 1-6 ng/mL.
    The specific activity of recombinant human VEGF165 is approximately 1.7 x 103 U/μg, which is calibrated against recombinant human VEGF165 WHO Standard (NIBSC code: 02/286).
  • Source
    Spodoptera frugiperda, Sf 9 (baculovirus)-derived Met1-Arg191 Produced in an animal component free process (ACFP).
    Manufactured and tested under cGMP guidelines.
  • Accession #
  • N-terminal Sequence
    Analysis
    Ala27-Pro-Met-Ala-Glu-Gly-Gly-Gly-Gln-Asn
  • Structure / Form
    Disulfide-linked homodimer
  • Predicted Molecular Mass
    19.2 kDa (monomer)
  • SDS-PAGE
    19-21 kDa, reducing conditions
293-GMP
 
Formulation Lyophilized from a 0.2 μm filtered solution in HCl.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS. Alternatively, reconstitute at 500 μg/mL in sterile 4 mM HCl.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • A minimum of 12 months when stored at ≤ -20 °C as supplied. Refer to lot specific COA for the Use by Date.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Data Images
GMP-grade Recombinant Human VEGF165 (Catalog # 293-GMP) stimulates proliferation in HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 1-6 ng/mL.
1 μg/lane of GMP-grade Recombinant Human VEGF 165 (Catalog # 293-GMP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 21 and 23 kDa and 39 kDa, respectively.
Background: VEGF

Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1-3). It is a member of the PDGF family that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure (4). Humans express alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4). VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189 (3, 4). Isoforms other than VEGF121 contain basic heparin-binding regions and are not freely diffusible (4). Human VEGF165 shares 88% aa sequence identity with corresponding regions of mouse and rat, 96% with porcine, 95% with canine, and 93% with feline, equine and bovine VEGF, respectively. VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR) on endothelial cells (4). Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). VEGF165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation with VEGF R2 (5). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4). In adults, VEGF functions mainly in wound healing and the female reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (6, 7). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (8). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 9).

  • References:
    1. Leung, D.W. et al. (1989) Science 246:1306. 
    2. Keck, P.J. et al. (1989) Science 246:1309. 
    3. Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777. 
    4. Robinson, C.J. and S.E. Stringer (2001) J. Cell. Sci. 114:853.
    5. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
    6. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
    7. Thurston, G. (2002) J. Anat. 200:575.
    8. Carvalho, J.F. et al. (2007) J. Clin. Immunol. 27:246.
    9. Angelo, L.S. and R. Kurzrock (2007) Clin. Cancer Res. 13:2825.
  • Long Name:
    Vascular Endothelial Growth Factor
  • Entrez Gene IDs:
    7422 (Human); 22339 (Mouse); 83785 (Rat); 281572 (Bovine); 403802 (Canine); 493845 (Feline); 30682 (Zebrafish)
  • Alternate Names:
    MVCD1; VAS; vascular endothelial growth factor A; Vascular permeability factor; Vasculotropin; VEGF; VEGFA; VEGF-A; VEGFMGC70609; VPF; VPFvascular endothelial growth factor

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